Evidence map›Paper›PMID 21905048›Full record

ArticleElectrophoresis2011

Chemical modification of proteins to improve the accuracy of their relative molecular mass determination by electrophoresis.

Vladislav Dolnik, William A Gurske

Abstract read
In one paragraph

Article in Electrophoresis, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Vladislav DolnikAlcor BioSeparations LLC, Palo Alto, CA, USA. ladia@dolnik.net
William A Gurske

Funding

Capillary sieving electrophoresis with a cationic surfactant for size-separationsR43GM085935 · NIGMS · ALCOR BIOSEPARATIONS · PI DOLNIK, VLADISLAV · 2009 to 2010
$448k
NIGMS NIH HHS 5 R43 GM085935-02NIGMS NIH HHS R43 GM085935
6 · The paper itself

Abstract

We studied the electrophoretic behavior of basic proteins (cytochrome c and histone III) and developed a carbamylation method that normalizes their electrophoretic size separation and improves the accuracy of their relative molecular mass determined electrophoretically. In capillary zone electrophoresis with cationic hitchhiking, native cytochrome c does not sufficiently bind cationic surfactants due to electrostatic repulsion between the basic protein and cationic surfactant. Carbamylation suppresses the strong positive charge of the basic proteins and results in more accurate relative molecular masses.

Indexed as

AnimalsBiochemical PhenomenaCationsCattleCytochromes cElectrophoresis, CapillaryHydrophobic and Hydrophilic InteractionsMolecular WeightPhosphinesProteinsCationsCytochromes cPhosphinesProteinstris(2-carboxyethyl)phosphine

Identifiers

PMID21905048
PMCPMC3516873
OpenAlexW2012504262

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.